Adsorption of the Enantiomers of Tryptophan on Stationary Phase Bonded with Bovine Serum Albumin

Frontal analysis is frequently applied to measuring single or multi-component adsorption isotherms. In this work, the competitive adsorption isotherm data of two enantiomers of tryptophan were obtained by competitive frontal analysis. The stationary phase in the column was silica-immobilized bovine serum albumin (BSA) by the derivative method, and the mobile phase was a phosphate buffer. These isotherm data were fitted by the competitive Bilangmuir model. This model can account for the behavior of both tryptophan enantiomers and these profiles were found to fit the experimental band profiles (square error is 0.999 6). The parameters obtained were used in numerical calculations to predict the band profiles of the racemic mixtures of tryptophan. The equilibrium-dispersive model provides satisfactory prediction, with minor differences between the calculated and the experimental profiles.